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B7H305 (LSPA_ACIB3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lipoprotein signal peptidase

EC=3.4.23.36
Alternative name(s):
Prolipoprotein signal peptidase
Signal peptidase II
Short name=SPase II
Gene names
Name:lspA
Ordered Locus Names:ABBFA_003491
OrganismAcinetobacter baumannii (strain AB307-0294) [Complete proteome] [HAMAP]
Taxonomic identifier557600 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This protein specifically catalyzes the removal of signal peptides from prolipoproteins By similarity. HAMAP MF_00161

Catalytic activity

Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains. HAMAP MF_00161

Pathway

Protein modification; lipoprotein biosynthesis (signal peptide cleavage). HAMAP MF_00161

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_00161.

Sequence similarities

Belongs to the peptidase A8 family.

Ontologies

Keywords
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionAspartyl protease
Hydrolase
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 176176Lipoprotein signal peptidase HAMAP MF_00161
PRO_1000190785

Regions

Transmembrane10 – 3021Helical; Potential
Transmembrane48 – 6821Helical; Potential
Transmembrane78 – 9821Helical; Potential
Transmembrane102 – 12221Helical; Potential
Transmembrane141 – 16121Helical; Potential

Sites

Active site1221 By similarity
Active site1491 By similarity

Sequences

Sequence LengthMass (Da)Tools
B7H305 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: CE10C08C4733E40A

FASTA17619,911
        10         20         30         40         50         60 
MPNSQAKKGL FQFYPHNLIW LGLSVLAIVL DQWTKWIAST HLNYADPVPV LPFLNWTLLH 

        70         80         90        100        110        120 
NYGAAFSFLS DAGGWQRYFF TSLAGLVSIL FVFWLLRMPK KMVVLPVAIA LILGGALGNL 

       130        140        150        160        170 
IDRITLGYVV DFIHVYYQNH HFPAFNIADS AITLGTILLL IDTFFLEKQR PKNSDA 

« Hide

References

[1]"Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii."
Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R.
J. Bacteriol. 190:8053-8064(2008) [PubMed: 18931120] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AB307-0294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001172 Genomic DNA. Translation: ACJ58527.1.
RefSeqYP_002327363.1. NC_011595.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB7H305.

Protein family/group databases

MEROPSA08.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7060639.
GenomeReviewsGene locus ABBFA_003491 in contig CP001172_GR.
KEGGabb:ABBFA_003491.
PATRIC20708453. VBIAciBau42682_3373.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG724422.
OMAMATRNNG.
ProtClustDBPRK00376.

Family and domain databases

HAMAPMF_00161. LspA.
[Tree]
InterProIPR001872. Peptidase_A8.
[Graphical view]
KOK03101.
PfamPF01252. Peptidase_A8. 1 hit.
[Graphical view]
PRINTSPR00781. LIPOSIGPTASE.
TIGRFAMsTIGR00077. LspA. 1 hit.
PROSITEPS00855. SPASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLSPA_ACIB3
AccessionPrimary (citable) accession number: B7H305
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families